A method for quantifying how the activity of an enzyme is affected by the net charge of its nearest crowded neighbor-Reference-Cited by-同舟云学术

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A method for quantifying how the activity of an enzyme is affected by the net charge of its nearest crowded neighbor

Published:2022-08-11 Issue:9 Volume:31 Page:
ISSN:0961-8368
Container-title:Protein Science
language:en
Short-container-title:Protein Science

Author:

Koone Jordan C.¹^ORCID,Dashnaw Chad M.¹,Gonzalez Mayte¹,Shaw Bryan F.¹^ORCID

Affiliation:

1. Department of Chemistry and Biochemistry Baylor University Waco Texas USA

Funder

National Science Foundation of Sri Lanka

Welch Foundation

Publisher

Wiley

Subject

Molecular Biology,Biochemistry

Link

https://onlinelibrary.wiley.com/doi/pdf/10.1002/pro.4384

Reference95 articles.

1. Energetics of enzyme catalysis.

2. Protein electrostatics: From computational and structural analysis to discovery of functional fingerprints and biotechnological design

3. Do Dynamic Effects Play a Significant Role in Enzymatic Catalysis? A Theoretical Analysis of Formate Dehydrogenase

4. Catalysis by dihydrofolate reductase and other enzymes arises from electrostatic preorganization, not conformational motions

5. Dynamic and Electrostatic Effects on the Reaction Catalyzed by HIV-1 Protease

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1. Harnessing Water Competition to Drive Enzyme Crosstalk;Biomacromolecules;2024-08-16

2. Charge Regulation in a Rieske Proton Pump Pinpoints Zero, One, and Two Proton-Coupled Electron Transfer;Journal of the American Chemical Society;2023-07-24

3. Quantification of carboxylate‐bridged di‐zinc site stability in protein due ferri by single‐molecule force spectroscopy;Protein Science;2023-02-14

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